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P09110 (THIK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-ketoacyl-CoA thiolase, peroxisomal

EC=2.3.1.16
Alternative name(s):
Acetyl-CoA acyltransferase
Beta-ketothiolase
Peroxisomal 3-oxoacyl-CoA thiolase
Gene names
Name:ACAA1
Synonyms:ACAA, PTHIO
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.

Pathway

Lipid metabolism; fatty acid metabolism.

Subunit structure

Homodimer. Ref.10

Subcellular location

Peroxisome.

Induction

Peroxisomal thiolase is markedly induced (at the level of transcription) by various hypolipidemic compounds in parallel with the other two enzymes of the peroxisomal beta-oxidation system.

Sequence similarities

Belongs to the thiolase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentPeroxisome
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransit peptide
   Molecular functionAcyltransferase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processalpha-linolenic acid metabolic process

Traceable author statement. Source: Reactome

bile acid metabolic process

Inferred from mutant phenotype PubMed 2318981. Source: UniProtKB

cellular lipid metabolic process

Traceable author statement. Source: Reactome

fatty acid beta-oxidation

Inferred from mutant phenotype PubMed 2365812PubMed 2882519. Source: UniProtKB

fatty acid beta-oxidation using acyl-CoA oxidase

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

unsaturated fatty acid metabolic process

Traceable author statement. Source: Reactome

very long-chain fatty acid metabolic process

Inferred from mutant phenotype PubMed 2318981. Source: UniProtKB

   Cellular_componentintracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

peroxisomal matrix

Traceable author statement. Source: Reactome

peroxisome

Inferred from direct assay PubMed 1347505PubMed 17881773PubMed 2365812PubMed 2895531PubMed 9053548. Source: UniProtKB

   Molecular_functionacetyl-CoA C-acyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

palmitoyl-CoA oxidase activity

Inferred from mutant phenotype PubMed 2882519. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P09110-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P09110-2)

The sequence of this isoform differs from the canonical sequence as follows:
     149-181: Missing.
     272-331: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2626Peroxisome
Chain27 – 4243983-ketoacyl-CoA thiolase, peroxisomal
PRO_0000034067

Sites

Active site1231Acyl-thioester intermediate By similarity
Active site3771Proton acceptor By similarity
Active site4081Proton acceptor By similarity

Amino acid modifications

Modified residue591Phosphothreonine Ref.8
Modified residue601Phosphothreonine Ref.8

Natural variations

Alternative sequence149 – 18133Missing in isoform 2.
VSP_046195
Alternative sequence272 – 33160Missing in isoform 2.
VSP_046196
Natural variant1721E → D.
Corresponds to variant rs156265 [ dbSNP | Ensembl ].
VAR_011904
Natural variant3871V → A. Ref.7
Corresponds to variant rs2229528 [ dbSNP | Ensembl ].
VAR_069148

Secondary structure

................................................................... 424
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1989. Version 2.
Checksum: 71B2BBAFA06AE412

FASTA42444,292
        10         20         30         40         50         60 
MQRLQVVLGH LRGPADSGWM PQAAPCLSGA PQASAADVVV VHGRRTAICR AGRGGFKDTT 

        70         80         90        100        110        120 
PDELLSAVMT AVLKDVNLRP EQLGDICVGN VLQPGAGAIM ARIAQFLSDI PETVPLSTVN 

       130        140        150        160        170        180 
RQCSSGLQAV ASIAGGIRNG SYDIGMACGV ESMSLADRGN PGNITSRLME KEKARDCLIP 

       190        200        210        220        230        240 
MGITSENVAE RFGISREKQD TFALASQQKA ARAQSKGCFQ AEIVPVTTTV HDDKGTKRSI 

       250        260        270        280        290        300 
TVTQDEGIRP STTMEGLAKL KPAFKKDGST TAGNSSQVSD GAAAILLARR SKAEELGLPI 

       310        320        330        340        350        360 
LGVLRSYAVV GVPPDIMGIG PAYAIPVALQ KAGLTVSDVD IFEINEAFAS QAAYCVEKLR 

       370        380        390        400        410        420 
LPPEKVNPLG GAVALGHPLG CTGARQVITL LNELKRRGKR AYGVVSMCIG TGMGAAAVFE 


YPGN 

« Hide

Isoform 2 [UniParc].

Checksum: 8137A0AC448FBA24
Show »

FASTA33134,665

References

« Hide 'large scale' references
[1]"Nucleotide sequence of human peroxisomal 3-oxoacyl-CoA thiolase."
Bout A., Teunissen Y., Hashimoto T., Benne R., Tager J.M.
Nucleic Acids Res. 16:10369-10369(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[2]Bout A.
Submitted (AUG-1989) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 285-287.
[3]"Complete cDNA sequence of human foetal liver peroxisomal 3-oxoacyl-CoA thiolase."
Fairbairn L.J., Tanner M.J.A.
Nucleic Acids Res. 17:3588-3588(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[4]"Characterization of the gene encoding human peroxisomal 3-oxoacyl-CoA thiolase (ACAA). No large DNA rearrangement in a thiolase-deficient patient."
Bout A., Franse M.M., Collins J., Blonden L., Tager J.M., Benne R.
Biochim. Biophys. Acta 1090:43-51(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT ALA-387.
Tissue: Lymph, Ovary and Pancreas.
[8]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-59 AND THR-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Crystal structure of human peroxisomal acetyl-COA acyl transferase 1 (ACAA1)."
Structural genomics consortium (SGC)
Submitted (OCT-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 28-424, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X12966 mRNA. Translation: CAA31412.1.
X14813 mRNA. Translation: CAA32918.1.
X65140 Genomic DNA. Translation: CAA46270.1.
X65148 Genomic DNA. Translation: CAA46271.1.
AP006309 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64516.1.
BC000635 mRNA. Translation: AAH00635.1.
BC011977 mRNA. Translation: AAH11977.1.
BC014474 mRNA. Translation: AAH14474.1.
PIRXUHUAB. S17515.
RefSeqNP_001123882.1. NM_001130410.1.
NP_001598.1. NM_001607.3.
UniGeneHs.643487.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IIKX-ray2.55A/B30-423[»]
ProteinModelPortalP09110.
SMRP09110. Positions 28-424.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106548. 18 interactions.
IntActP09110. 1 interaction.
MINTMINT-3006670.
STRING9606.ENSP00000333664.

PTM databases

PhosphoSiteP09110.

Polymorphism databases

DMDM135751.

2D gel databases

REPRODUCTION-2DPAGEIPI00012828.
UCD-2DPAGEP09110.

Proteomic databases

PaxDbP09110.
PeptideAtlasP09110.
PRIDEP09110.

Protocols and materials databases

DNASU30.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301810; ENSP00000301810; ENSG00000060971. [P09110-2]
ENST00000333167; ENSP00000333664; ENSG00000060971. [P09110-1]
GeneID30.
KEGGhsa:30.
UCSCuc003cht.3. human. [P09110-1]
uc003chu.3. human.

Organism-specific databases

CTD30.
GeneCardsGC03M038164.
HGNCHGNC:82. ACAA1.
HPAHPA006764.
HPA007244.
MIM604054. gene.
neXtProtNX_P09110.
PharmGKBPA24419.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0183.
HOGENOMHOG000012239.
HOVERGENHBG003112.
InParanoidP09110.
KOK07513.
OMAMEHKDAT.
OrthoDBEOG7K3TM6.
PhylomeDBP09110.
TreeFamTF332308.

Enzyme and pathway databases

BioCycMetaCyc:HS00752-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00199.

Gene expression databases

ArrayExpressP09110.
BgeeP09110.
CleanExHS_ACAA1.
GenevestigatorP09110.

Family and domain databases

Gene3D3.40.47.10. 4 hits.
InterProIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PANTHERPTHR18919. PTHR18919. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMSSF53901. SSF53901. 2 hits.
TIGRFAMsTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSACAA1. human.
EvolutionaryTraceP09110.
GeneWikiACAA1.
GenomeRNAi30.
NextBio107.
PROP09110.
SOURCESearch...

Entry information

Entry nameTHIK_HUMAN
AccessionPrimary (citable) accession number: P09110
Secondary accession number(s): G5E935, Q96CA6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1989
Last modified: April 16, 2014
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM